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B2HR81 (SYR_MYCMM) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 36. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Arginine--tRNA ligase

EC=6.1.1.19
Alternative name(s):
Arginyl-tRNA synthetase
Short name=ArgRS
Gene names
Name:argS
Ordered Locus Names:MMAR_4105
OrganismMycobacterium marinum (strain ATCC BAA-535 / M) [Complete proteome] [HAMAP]
Taxonomic identifier216594 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length550 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg). HAMAP-Rule MF_00123

Subunit structure

Monomer By similarity. HAMAP-Rule MF_00123

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00123.

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processarginyl-tRNA aminoacylation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

arginine-tRNA ligase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 550550Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_1000095383

Regions

Motif130 – 14011"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
B2HR81 [UniParc].

Last modified June 10, 2008. Version 1.
Checksum: 2FE3FEE20599A93C

FASTA55059,679
        10         20         30         40         50         60 
MTPADLAELL KSTATAVLSE HALDTSALPQ TVVVERPRNP EHGDYASNVA LQLAKKVGAN 

        70         80         90        100        110        120 
PRELAGWIAE ALTKADGIAS AEVAGPGFIN LRLETSAQAK IVNAIIDAGS GFGHSELMAA 

       130        140        150        160        170        180 
HKVNLEFVSA NPTGPIHIGG TRWAAVGDAL GRLLSTQGAD VVREYYFNDH GAQIDRFANS 

       190        200        210        220        230        240 
LIAAAKGEPT PDDGYAGTYI NDIAARVLQK APDALSLPDA QMHETFREIG VDLMFSHIKE 

       250        260        270        280        290        300 
SLHEFGTDFD VYTHEDSMHS TGRVDQAVAR LRETGNIYEK DGATWLRSSS FGDDKDRVVI 

       310        320        330        340        350        360 
KSDGKPAYIA GDLAYYLDKR ERGFDLCIYM LGADHHGYIA RLKAAAAAFG EDPATVEVLI 

       370        380        390        400        410        420 
GQMVNLVRDG QPVRMSKRAG TVITLDDLVE AIGVDAARYS LIRSSVDTPI DIDLALWSSA 

       430        440        450        460        470        480 
SNENPVYYVQ YAHARLSALA RNAAELGLIP DTDHLELLSH EKEGVLLRTL GDFPRMLKTA 

       490        500        510        520        530        540 
ASLREPHRVC RYLEDLAGDY HRFYDSCRVL PQGDEEPTQL HTARLALCQA TRQVIANGLG 

       550 
ILGVTAPERM 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000854 Genomic DNA. Translation: ACC42512.1.
RefSeqYP_001852367.1. NC_010612.1.

3D structure databases

ProteinModelPortalB2HR81.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING216594.MMAR_4105.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACC42512; ACC42512; MMAR_4105.
GeneID6228384.
KEGGmmi:MMAR_4105.
PATRIC18069461. VBIMycMar75906_4398.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247214.
KOK01887.
OMANPNGPLH.
OrthoDBEOG6JB13C.
ProtClustDBPRK01611.

Enzyme and pathway databases

BioCycMMAR216594:GJOB-4135-MONOMER.

Family and domain databases

Gene3D1.10.730.10. 1 hit.
3.30.1360.70. 1 hit.
3.40.50.620. 1 hit.
HAMAPMF_00123. Arg_tRNA_synth.
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR001278. Arg-tRNA-ligase.
IPR005148. Arg-tRNA-synth_N.
IPR008909. DALR_anticod-bd.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009080. tRNAsynth_1a_anticodon-bd.
[Graphical view]
PANTHERPTHR11956. PTHR11956. 1 hit.
PfamPF03485. Arg_tRNA_synt_N. 1 hit.
PF05746. DALR_1. 1 hit.
PF00750. tRNA-synt_1d. 1 hit.
[Graphical view]
PRINTSPR01038. TRNASYNTHARG.
SMARTSM01016. Arg_tRNA_synt_N. 1 hit.
SM00836. DALR_1. 1 hit.
[Graphical view]
SUPFAMSSF47323. SSF47323. 1 hit.
SSF55190. SSF55190. 1 hit.
TIGRFAMsTIGR00456. argS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYR_MYCMM
AccessionPrimary (citable) accession number: B2HR81
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: June 10, 2008
Last modified: April 16, 2014
This is version 36 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries